Stress-induced phosphoprotein (STIP1, SEQ ID NO:3) is a 62.6 kDa protein, also known as heat shock protein (HSP)-organizing protein (HOP), because it has been shown to modulate the chaperone activities of HSP 90 and HSP 70. STIP1 contains nine tetratricopeptide repeat (TPR) motifs and one nuclear localization signal (NLS) (Longshaw et al., 2004). The TPR domains of STIP1 are involved in holding HSP70 and HSP90 together in the HSP90 chaperone machinery (Odunuga et al., 2004). This formation of protein complexes participates in several cellular processes, including transcription, protein folding, protein translocation, viral replication, signal transduction, and cell division.
Cancer remains a major public health problem worldwide. It profoundly affects more than 1 million people in the U.S. diagnosed each year, as well as their families and friends. Despite the advance in chemotherapy over the last 50 years, the medical community is still faced with the challenge for curing many different types of cancer. Accordingly, there is still a need for the development of effective and safe treatments for various types of cancer. The present invention addresses this need.